ExplorEnz: EC 1.14.11.45

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1.14.11.45

Accepted name:

L-isoleucine 4-hydroxylase

Reaction:

L-isoleucine + 2-oxoglutarate + O₂ = (4S)-4-hydroxy-L-isoleucine + succinate + CO₂

Glossary:

(4S)-4-hydroxy-L-isoleucine = (2S,3R,4S)-2-amino-4-hydroxy-3-methylpentanoate

Other name(s):

ido (gene name)

Systematic name:

L-isoleucine,2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating)

Comments:

The enzyme, characterized from the bacterium Bacillus thuringiensis, can also catalyse the hydroxylation of L-leucine, L-norvaline, L-norleucine, and L-allo-isoleucine, as well as the sulfoxidation of L-methionine, L-ethionine, S-methyl-L-cysteine, S-ethyl-L-cysteine, and S-allyl-L-cysteine.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Kodera, T., Smirnov, S.V., Samsonova, N.N., Kozlov, Y.I., Koyama, R., Hibi, M., Ogawa, J., Yokozeki, K. and Shimizu, S. A novel L-isoleucine hydroxylating enzyme, L-isoleucine dioxygenase from Bacillus thuringiensis, produces (2S,3R,4S)-4-hydroxyisoleucine. Biochem. Biophys. Res. Commun. 390 (2009) 506–510. [DOI] [PMID: 19850012]
2.	Hibi, M., Kawashima, T., Kodera, T., Smirnov, S.V., Sokolov, P.M., Sugiyama, M., Shimizu, S., Yokozeki, K. and Ogawa, J. Characterization of Bacillus thuringiensis L-isoleucine dioxygenase for production of useful amino acids. Appl. Environ. Microbiol. 77 (2011) 6926–6930. [DOI] [PMID: 21821743]
3.	Hibi, M., Kawashima, T., Yajima, H., Smirnov, S.V., Kodera, T., Sugiyama, M., Shimizu, S., Yokozeki, K., and Ogawa, J. Enzymatic synthesis of chiral amino acid sulfoxides by Fe(II)/α ketoglutarate-dependent dioxygenase. Tetrahedron Asym. 24 (2013) 990–994.

[EC 1.14.11.45 created 2014]